Accession Number:

ADA463672

Title:

Role of Rad23 and Dsk2 in Nucleotide Excision Repair and Spindle Pole Body Duplication

Descriptive Note:

Annual summary rept. 28 Feb 2005-27 Feb 2006

Corporate Author:

MINNESOTA UNIV MINNEAPOLIS

Personal Author(s):

Report Date:

2006-03-01

Pagination or Media Count:

17.0

Abstract:

The three yeast UBL-UBA proteins, Rad23, Ddi1 and Dsk2 bind both ubiquitin and the proteasome. They are not essential for viability and some redundancy in terms of stabilization of ubiquitinated substrates has been shown, suggesting that they may have overlapping functions. Here we showed that Rad23 is indeed redundant with both Ddi1 and Dsk2 for cell cycle related roles. Surprisingly, Ddi1 and Dsk2 do not show any redundancy but the triple deletion shows an synthetic defect, suggesting that Rad23 has at least two different roles in cell cycle progression during G2M. In addition, we found that these putative roles do not include a role in SPB duplication, which contradicts a previously reported study 3. We do not know at the time the nature of this discrepancy. In addition, we show that a tetra-ubiquitin chain is able to bind several UBL-UBA proteins at once, which might explain the redundancies observed, as well as suggesting that these multiple interactions might be relevant for efficient but regulated delivery of ubiquitinated substrates to the proteasome.

Subject Categories:

  • Biochemistry
  • Genetic Engineering and Molecular Biology
  • Medicine and Medical Research

Distribution Statement:

APPROVED FOR PUBLIC RELEASE